JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M100506200 on July 6, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33645-33651, September 7, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/36/33645    most recent
M100506200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lensch, M.
Right arrow Articles by Sokolenko, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lensch, M.
Right arrow Articles by Sokolenko, A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Identification and Characterization of SppA, a Novel Light-inducible Chloroplast Protease Complex Associated with Thylakoid Membranes*

Martin Lensch, Reinhold G. Herrmann, and Anna SokolenkoDagger

From the Botanisches Institut der Ludwig-Maximilians-Universität, Menzingerstrasse 67, D-80638 München, Germany

A new component of the chloroplast proteolytic machinery from Arabidopsis thaliana was identified as a SppA-type protease. The sequence of the mature protein, deduced from a full-length cDNA, displays 22% identity to the serine-type protease IV (SppA) from Escherichia coli and 27% identity to Synechocystis SppA1 (sll1703) but lacks the putative transmembrane spanning segments predicted from the E. coli sequence. The N-terminal sequence exhibits typical features of a cleavable chloroplast stroma-targeting sequence. The chloroplast localization of SppA was confirmed by in organello import experiments using an in vitro expression system and by immunodetection with antigen-specific antisera. Subfractionation of intact chloroplasts demonstrated that SppA is associated exclusively with thylakoid membranes, predominantly stroma lamellae, and is a part of some high molecular mass complex of about 270 kDa that exhibits proteolytic activity. Treatments with chaotropic salts and proteases showed that SppA is largely exposed to the stroma but that it behaves as an intrinsic membrane protein that may have an unusual monotopic arrangement in the thylakoids. We demonstrate that SppA is a light-inducible protease and discuss its possible involvement in the light-dependent degradation of antenna and photosystem II complexes that both involve serine-type proteases.

* This work was supported by Deutsche Forschungsgemeinschaft Grant DFG SO448/2-1 (to A. S.) and SFB 184 (to R. H.) and the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 49-89-17861242; Fax: 49-89-1782274; E-mail: anna@botanik.biologie.uni-muenchen.d.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol Biol EvolHome page
T. Nosenko, K. L. Lidie, F. M. Van Dolah, E. Lindquist, J.-F. Cheng, US Department of Energy-Joint Genome Institute, and D. Bhattacharya
Chimeric Plastid Proteome in the Florida "Red Tide" Dinoflagellate Karenia brevis
Mol. Biol. Evol., November 1, 2006; 23(11): 2026 - 2038.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
A. Rudella, G. Friso, J. M. Alonso, J. R. Ecker, and K. J. van Wijk
Downregulation of ClpR2 Leads to Reduced Accumulation of the ClpPRS Protease Complex and Defects in Chloroplast Biogenesis in Arabidopsis
PLANT CELL, July 1, 2006; 18(7): 1704 - 1721.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
L. Giacomelli, A. Rudella, and K. J. van Wijk
High Light Response of the Thylakoid Proteome in Arabidopsis Wild Type and the Ascorbate-Deficient Mutant vtc2-2. A Comparative Proteomics Study
Plant Physiology, June 1, 2006; 141(2): 685 - 701.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Zelisko, M. Garcia-Lorenzo, G. Jackowski, S. Jansson, and C. Funk
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
PNAS, September 20, 2005; 102(38): 13699 - 13704.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
E. Pojidaeva, V. Zinchenko, S. V. Shestakov, and A. Sokolenko
Involvement of the SppA1 Peptidase in Acclimation to Saturating Light Intensities in Synechocystis sp. Strain PCC 6803
J. Bacteriol., June 15, 2004; 186(12): 3991 - 3999.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. N. Henderson, J. Zhang, B. W. Evans, and K. Redding
Disassembly and Degradation of Photosystem I in an in Vitro System Are Multievent, Metal-dependent Processes
J. Biol. Chem., October 10, 2003; 278(41): 39978 - 39986.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
Y. Chassin, E. Kapri-Pardes, G. Sinvany, T. Arad, and Z. Adam
Expression and Characterization of the Thylakoid Lumen Protease DegP1 from Arabidopsis
Plant Physiology, October 1, 2002; 130(2): 857 - 864.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.